ID A0A136MD92_9BACT Unreviewed; 1051 AA.
AC A0A136MD92;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN Name=recB {ECO:0000313|EMBL:KXK31864.1};
GN ORFNames=UZ16_OP3001002726 {ECO:0000313|EMBL:KXK31864.1};
OS Candidatus Hinthialibacteria bacterium OLB16.
OC Bacteria; Candidatus Hinthialibacterota.
OX NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK31864.1, ECO:0000313|Proteomes:UP000070296};
RN [1] {ECO:0000313|EMBL:KXK31864.1, ECO:0000313|Proteomes:UP000070296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OLB16 {ECO:0000313|EMBL:KXK31864.1};
RA Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT "Genome based microbial ecology of anammox granules in a full-scale
RT wastewater treatment system.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXK31864.1}.
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DR EMBL; LMZT01000139; KXK31864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A136MD92; -.
DR STRING; 1617433.UZ16_OP3001002726; -.
DR PATRIC; fig|1617433.3.peg.2926; -.
DR Proteomes; UP000070296; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0008854; F:exodeoxyribonuclease V activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd22352; RecB_C-like; 1.
DR Gene3D; 3.90.320.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR HAMAP; MF_01485; RecB; 1.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR038726; PDDEXK_AddAB-type.
DR InterPro; IPR004586; RecB.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF23; RECBCD ENZYME SUBUNIT RECB; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF12705; PDDEXK_1; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}.
FT DOMAIN 1..318
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 330..617
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
FT BINDING 15..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00560"
SQ SEQUENCE 1051 AA; 120292 MW; 77C3BAD62D5B2DDF CRC64;
MSLDIDLSKH ALIEASAGTG KTFTIETLVV QLLVEKQIPL SQILLVTFTE KATSEMKARI
RKKLDSLIKE GISQPNVVES LIQFDQAQVM TIHSFCKQIL QQYSLENGIL FDLDLTDTAS
LYLAGLRDIQ RKWSARERDI LDSSVYRDQD KIKNWEEMVV RYAHDYNKAS GDVFSTADDK
PDNVAWHEFT ADLIKTLHQQ VCEQAREKGL ASFDDLLRLV DEALHQESTA SQRLLESIRS
QYRYAFVDEF QDTDPVQWRI FKKIFIDHKQ LNRLFLVGDP KQSIYRFRGA DIFTYLSARE
TLKQLGEIYE LDKNWRSTPD LITFQNWIFS SSWFPAESGI AYPPVQPPKE DSTGKRPFAC
DNSKRKSAVF LSLPKLSATE LRQCYARWIV TEIRYLLGMD DNGDPLITFP GHEGKSRPFK
PGDICVLVNT RNEGDIVARQ LEGIVPYSFY KKTGLYASEE ALHLFYLLDA LSNPECSTRR
QRALLTDFFQ IPLDAFNQQD VSSTHSLQIS LIDKWCDLAA SRKWTHLFDS IQNQSLVFFR
IGEVMKAPDD RSIANYKHLF EDLLMIACDS MMDIEMLTQH FDRKRRARIM IDREEDLHRI
DSDQSKVQLM TIHASKGLEY PVVFLGGLSP GKTRDSSDFY HENGAKVFRL GESSREKELA
QNELADEQRR LYYVAITRAM NRVYIPLIEG CELRGNQGPI VSISDIPPAL SQTCGMIELV
PDAILSAYRQ LVPVASHSNG GPPEDFISPD IRRIKASGIH ISSFSSLHHS NLAQPQILIA
RDYDDEPPFS AVDDVTDSMD AVVPSEDPLP PGAHTGDMLH AIFQSIPFDE VAAAASPEEL
LHTTTRSLKV ISQAFAQSDL YRKLDPSEHH KCIERIANII WNTLKVPPGE EIQYPPLATI
PERDRRHEIE FHLSDDVIEK YLPDIFRKPN THCRRYLKGY IDLVFRFEGR YHIVDWKSNS
LHPFNQETIE QCIIDNQYDL QYTIYWAALV EWLKKILPDF DPEVHLGGVS YYFIRGIRMT
ESGKGIFHRS AADLSRNLQT AVVQTNPGSK L
//
